Organic And Biological Chemistry
7th Edition
ISBN: 9781305081079
Author: STOKER, H. Stephen (howard Stephen)
Publisher: Cengage Learning,
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Textbook Question
Chapter 10.6, Problem 1QQ
The number of substrate molecules converted to product per minute is a measure of
- a. enzyme activity
- b. enzyme concentration
- c. enzyme specificity
- d. no correct response
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24. In the following diagram, the rate of an enzyme-catalyzed reaction is graphed on the y (or vertical) axis versus another quantity on the x axis. What quantity is graphed
on the x axis?
a. substrate concentration
Ob. reaction pH
Oc. reaction temperature
Od. more than one response is correct
e. no correct response
22. According to the lock-and-key theory of enzyme behavior, which of the following can be thought of as the key?
a. enzyme
b. substrate
с. ароenzyme
d. coenzyme
e. no correct response
A non-reactive substrate analogue has been found to inhibit a
target enzyme. Modifying the inhibitor to make it more like TS
(‡) will? (Select All that Apply)
a. Make it a better inhibitor
b. Make it a worse inhibitor
c. Make it bind tighter
d. Make it bind weaker
e. Increase the KD
f. Decrease the KD
Chapter 10 Solutions
Organic And Biological Chemistry
Ch. 10.1 - Which of the following statements concerning the...Ch. 10.1 - Prob. 2QQCh. 10.2 - Which of the following statements about a...Ch. 10.2 - Which of the following statements about cofactors...Ch. 10.2 - Prob. 3QQCh. 10.3 - Which of the following statements concerning an...Ch. 10.3 - Most enzyme names end with the suffix ase, but a...Ch. 10.3 - Which of the following pairings of enzyme type and...Ch. 10.3 - Which of the following pairings of enzyme type and...Ch. 10.4 - An enzyme active site is the location in an enzyme...
Ch. 10.4 - Which of the following statements concerning the...Ch. 10.4 - Which of the following enzyme properties is...Ch. 10.5 - The specificity of an enzyme that catalyzes the...Ch. 10.5 - Linkage-specific enzymes will act on a particular...Ch. 10.6 - The number of substrate molecules converted to...Ch. 10.6 - Prob. 2QQCh. 10.6 - Prob. 3QQCh. 10.7 - Extremozyme presence is not possible in which of...Ch. 10.7 - Prob. 2QQCh. 10.8 - Which of the following statements concerning a...Ch. 10.8 - Which of the following statements concerning an...Ch. 10.8 - Which of the following binds to an enzyme at a...Ch. 10.9 - Which of the following is an incorrect...Ch. 10.9 - Prob. 2QQCh. 10.9 - Which of the following statements applies to a...Ch. 10.10 - Prob. 1QQCh. 10.10 - Prob. 2QQCh. 10.11 - Prob. 1QQCh. 10.11 - Prob. 2QQCh. 10.12 - Prob. 1QQCh. 10.12 - Prob. 2QQCh. 10.12 - Prob. 3QQCh. 10.13 - Prob. 1QQCh. 10.13 - Which of the following statements about...Ch. 10.13 - In the recharging of a metal-containing enzyme by...Ch. 10.14 - Prob. 1QQCh. 10.14 - Prob. 2QQCh. 10.14 - Prob. 3QQCh. 10.14 - Which of the B vitamins has a name that draws...Ch. 10.14 - Prob. 5QQCh. 10.14 - Prob. 6QQCh. 10.15 - Prob. 1QQCh. 10.15 - Prob. 2QQCh. 10.15 - Prob. 3QQCh. 10.15 - Prob. 4QQCh. 10.15 - Prob. 5QQCh. 10 - What is the general role of enzymes in the human...Ch. 10 - Prob. 10.2EPCh. 10 - List two ways in which enzymes differ from...Ch. 10 - Occasionally the delicate nature of enzymes is...Ch. 10 - Indicate whether each of the following phrases...Ch. 10 - Indicate whether each of the following phrases...Ch. 10 - Prob. 10.7EPCh. 10 - Prob. 10.8EPCh. 10 - Prob. 10.9EPCh. 10 - Prob. 10.10EPCh. 10 - Prob. 10.11EPCh. 10 - Based on its name, indicate whether each of the...Ch. 10 - Predict the function of each of the following...Ch. 10 - Predict the function of each of the following...Ch. 10 - Prob. 10.15EPCh. 10 - What is the substrate for each of the enzymes...Ch. 10 - Suggest a name for an enzyme that catalyzes each...Ch. 10 - Suggest a name for an enzyme that catalyzes each...Ch. 10 - Prob. 10.19EPCh. 10 - Indicate whether each of the following pairings of...Ch. 10 - Prob. 10.21EPCh. 10 - Prob. 10.22EPCh. 10 - Identify the enzyme needed in each of the...Ch. 10 - Identify the enzyme needed in each of the...Ch. 10 - Indicate whether each of the following statements...Ch. 10 - Indicate whether each of the following statements...Ch. 10 - Indicate whether each of the statements in Problem...Ch. 10 - Indicate whether each of the statements in Problem...Ch. 10 - Prob. 10.29EPCh. 10 - Prob. 10.30EPCh. 10 - Prob. 10.31EPCh. 10 - Prob. 10.32EPCh. 10 - Prob. 10.33EPCh. 10 - Indicate whether each of the following statements...Ch. 10 - Prob. 10.35EPCh. 10 - Prob. 10.36EPCh. 10 - Prob. 10.37EPCh. 10 - Prob. 10.38EPCh. 10 - What type of specificity (absolute, group,...Ch. 10 - What type of specificity (absolute, group,...Ch. 10 - The following graph shows the relationship between...Ch. 10 - Based on the graphical information in Problem...Ch. 10 - Prob. 10.43EPCh. 10 - Based on the graphical information in Problem...Ch. 10 - Prob. 10.45EPCh. 10 - Prob. 10.46EPCh. 10 - Prob. 10.47EPCh. 10 - Prob. 10.48EPCh. 10 - Prob. 10.49EPCh. 10 - Prob. 10.50EPCh. 10 - Describe the effect that each of the following...Ch. 10 - Prob. 10.52EPCh. 10 - Prob. 10.53EPCh. 10 - Prob. 10.54EPCh. 10 - Indicate whether each of the following pairings of...Ch. 10 - Indicate whether each of the following pairings of...Ch. 10 - Prob. 10.57EPCh. 10 - Prob. 10.58EPCh. 10 - Prob. 10.59EPCh. 10 - Prob. 10.60EPCh. 10 - Prob. 10.61EPCh. 10 - Indicate whether each of the following statements...Ch. 10 - Prob. 10.63EPCh. 10 - Indicate whether each of the following statements...Ch. 10 - Prob. 10.65EPCh. 10 - Prob. 10.66EPCh. 10 - Prob. 10.67EPCh. 10 - Prob. 10.68EPCh. 10 - Prob. 10.69EPCh. 10 - What occurs during the covalent modification of an...Ch. 10 - Prob. 10.71EPCh. 10 - Prob. 10.72EPCh. 10 - Explain the difference in meaning, if any, between...Ch. 10 - Prob. 10.74EPCh. 10 - Prob. 10.75EPCh. 10 - Prob. 10.76EPCh. 10 - Prob. 10.77EPCh. 10 - Prob. 10.78EPCh. 10 - Prob. 10.79EPCh. 10 - Prob. 10.80EPCh. 10 - Prob. 10.81EPCh. 10 - What enzyme is denoted by each of the following...Ch. 10 - What is the medical diagnostic value associated...Ch. 10 - What is the medical diagnostic value associated...Ch. 10 - Indicate whether each of the following is a...Ch. 10 - Indicate whether each of the following is a...Ch. 10 - Prob. 10.87EPCh. 10 - Indicate whether each of the vitamins in Problem...Ch. 10 - Prob. 10.89EPCh. 10 - Prob. 10.90EPCh. 10 - Prob. 10.91EPCh. 10 - What are the structural differences between the...Ch. 10 - Prob. 10.93EPCh. 10 - Prob. 10.94EPCh. 10 - Prob. 10.95EPCh. 10 - Prob. 10.96EPCh. 10 - Prob. 10.97EPCh. 10 - Only eight of the nine water-soluble vitamins are...Ch. 10 - Indicate whether each of the following B vitamin...Ch. 10 - Indicate whether each of the following B vitamin...Ch. 10 - Which of the B vitamins has a structure that fits...Ch. 10 - Prob. 10.102EPCh. 10 - Prob. 10.103EPCh. 10 - Prob. 10.104EPCh. 10 - Prob. 10.105EPCh. 10 - Prob. 10.106EPCh. 10 - The coenzyme forms of B vitamins are involved in...Ch. 10 - Prob. 10.108EPCh. 10 - Prob. 10.109EPCh. 10 - What is the relationship between the plant pigment...Ch. 10 - Prob. 10.111EPCh. 10 - Prob. 10.112EPCh. 10 - Prob. 10.113EPCh. 10 - Prob. 10.114EPCh. 10 - Prob. 10.115EPCh. 10 - In terms of their source, how do vitamin D2 and...Ch. 10 - Prob. 10.117EPCh. 10 - Why is vitamin D often called the sunshine...Ch. 10 - Prob. 10.119EPCh. 10 - Prob. 10.120EPCh. 10 - Prob. 10.121EPCh. 10 - Prob. 10.122EPCh. 10 - What is the principal function of vitamin E in the...Ch. 10 - Why is vitamin E often given to premature infants...Ch. 10 - Prob. 10.125EPCh. 10 - Prob. 10.126EPCh. 10 - Prob. 10.127EPCh. 10 - Prob. 10.128EPCh. 10 - Indicate whether each of the following pairings of...Ch. 10 - Indicate whether each of the following pairings of...Ch. 10 - Prob. 10.131EPCh. 10 - Prob. 10.132EPCh. 10 - Prob. 10.133EPCh. 10 - Which of the 13 vitamins has a structure that fits...
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- 6. An enzyme without its cofactor is inactive. Another name for an inactive enzyme of this type is a. isoenzyme b. allosteric enzyme с. ароenzyme d. more than one response is correct e. no correct responsearrow_forwardProblem 4 The hydrolysis of a substrate, S, by an enzyme has been studied in the lab. The following initial rates, vo, were recorded at different concentrations. [S] (M) Vo (M/min) 2.10-104 1.20- 106 4.20- 104 3.10- 106 6.30 - 105 9.10 - 106 9.30- 104 1.42-103 B. What is the rate of reaction at [S] = 1.1-104 M? 'arrow_forwardProblem 4 The hydrolysis of a substrate, S, by an enzyme has been studied in the lab. The following initial rates, vo, were recorded at different concentrations. [S] (M) 2.10- 104 Vo (M/min) 1.20 - 106 4.20. 104 3.10- 106 9.30- 104 6.30 - 106 1.42. 103 9.10- 106 C. Explain, why encyıies can make reactions go laster? Does enzymes also catalyse the reverse reaction from product to substrate?arrow_forward
- (b) Determine how the reaction rate varies with substrate concentration. Rate increases substrate is added when enzyme is saturated with substrate Incorrect Rate decreases additional substrate is added when substrate concentration is low Answer Bank Rate is unchanged additional substrate is added when substrate concentration is very higharrow_forwardProblem 1. At the given temperature, experimental data for enzyme-catalyzed reaction rates were obtained as follows. Answer the following questions. The initially added enzyme concentration, [E.], was 2 mol/L. The reaction rates in the absence and the presence of an inhibitor were measured. The concentration of the inhibitor was 0.5 mol/L. [S] (mol/L) v (no inhibitor) (mol/L-min) v (inhibitor presence) (mol/L.min) 0.1 3.7 0.05 3.0 0.03 2.5 0.015 1.8 0.005 0.7 1.3 1.2 1.1 0.9 0.5 a. Calculate the values of Km and Vm in the absence of the inhibitor. b. Calculate the value of K₁ in the presence of the inhibitor. c. Draw the catalytic mechanism of the reaction in the presence of the inhibitor. d. Identify the type of inhibitor.arrow_forwardProblem 4 The hydrolysis of a substrate, S, by an enzyme has been studied in the lab. The following initial rates, vo, were recorded at different concentrations. [S] (M) Vo (M/min) 2.10- 104 1.20- 106 4.20. 104 3.10. 106 9.30- 104 6.30 - 106 1.42- 103 9.10- 106 A. Determine the rate constants for degradation of the substrate.arrow_forward
- Problem 4 The hydrolysis of a substrate, S, by an enzyme has been studied in the lab. The following initial rates, vo, were recorded at different concentrations. [S] (M) Vo (M/min) 2.10. 104 1.20- 106 4.20- 104 3.10- 106 9.30. 104 6.30 - 105 1.42- 103 9.10- 106 A. Determine the rate constants for degradation of the substrate. B. What is the rate of reaction at [S] = 1.1-10“ M? C. Explain, why enzymes can make reactions go faster? Does enzymes also catalyse the reverse reaction from product to substrate?arrow_forwardAn enzyme has no activity at an extremely low pH. What could be an explanation for this observation? a. enzyme inhibition b. protein denaturation c. lack of cofactors d. substrate deactivation e. no correct response givenarrow_forwardThe complete hydrolysis of a protein yields what as products? a. amino acids b. dipeptides c. monosaccharides d. glucose molecules e. no correct response givenarrow_forward
- An experiment was performed to determine the effects of an inhibitor on the breakdown of glycogen by an enzyme. In an accompanying experiment, the inhibitor was added to the glycogen-enzyme suspension and reacted using the same experimental conditions. The data obtained from these experiments is tabulated below. Glycogen (mM) Product Formed Glycogen only (mM/min) Product Formed Glycogen and Inhibitor (mM/min) 0.5 22.6 15.9 1.0 32.1 24.9 1.5 38.1 28.2 2.0 41.2 35.1 2.5 44.7 40.0 3.0 48.5 43.3 Draw the Michaelis-Menten and Lineweaver-Burke plots of these dat In the attachment. Determine the form of inhibition observed from these results, and explain your rationale for this form. Determine the values for Km and Vmax from these results.arrow_forwardQuestion 17 You analyze the enzyme A's reaction. When vo is 9.6uM s1, Vmax is 480UM s and [S] is 40uM, what is the Km of this enzyme A? You do need to show the calculation. Edit View Insert Format Tools Tablearrow_forwardA transition-state analog ____. Select one: a. resembles the transition-state structure of the normal enzyme-substrate complex b. is less stable when binding to an enzyme than the normal substrate c. stabilizes the transition state for the normal enzyme-substrate complex d. typically reacts more rapidly with an enzyme than the normal substratearrow_forward
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